SitesBLAST
Comparing AO353_03310 FitnessBrowser__pseudo3_N2E3:AO353_03310 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
55% identity, 99% coverage: 2:562/566 of query aligns to 1:560/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E362) mutation to A: Loss of activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
32% identity, 89% coverage: 48:552/566 of query aligns to 47:534/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H262), F245 (≠ Y264), T249 (≠ H269), G314 (= G335), A315 (≠ M336), P316 (≠ A337), G337 (= G357), Y338 (= Y358), G339 (= G359), L340 (≠ M360), T341 (= T361), S345 (≠ P365), A346 (≠ V366), D420 (= D439), I432 (= I451), K527 (= K545)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y264), R335 (≠ C355), G337 (= G357), G339 (= G359), L340 (≠ M360), A346 (≠ V366)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
32% identity, 89% coverage: 48:552/566 of query aligns to 47:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H262), F245 (≠ Y264), T249 (≠ H269), G314 (= G335), A315 (≠ M336), P316 (≠ A337), G337 (= G357), Y338 (= Y358), G339 (= G359), L340 (≠ M360), T341 (= T361), A346 (≠ V366), D420 (= D439), I432 (= I451), K527 (= K545)
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 93% coverage: 24:551/566 of query aligns to 30:536/546 of Q84P21
- K530 (= K545) mutation to N: Lossed enzymatic activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 90% coverage: 47:553/566 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H262), T303 (= T361), E304 (= E362), I403 (≠ L460), N408 (= N465), A491 (≠ K545)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (≠ G216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H262), S277 (≠ G335), A278 (≠ M336), P279 (≠ A337), E298 (= E356), M302 (= M360), T303 (= T361), D382 (= D439), R397 (= R454)
- binding carbonate ion: H207 (= H262), S277 (≠ G335), R299 (≠ G357), G301 (= G359)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 94% coverage: 20:552/566 of query aligns to 9:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H262), T328 (= T361), E329 (= E362), K433 (≠ L460), Q438 (≠ N465), K518 (= K545)
- binding adenosine monophosphate: A301 (≠ G335), G326 (= G359), T328 (= T361), D412 (= D439), K429 (= K456), K433 (≠ L460), Q438 (≠ N465)
- binding coenzyme a: L102 (= L108), P226 (= P259), H229 (= H262), Y231 (= Y264), F253 (≠ R287), K435 (≠ S462), G436 (= G463), F437 (= F464), F498 (≠ G525)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
30% identity, 94% coverage: 20:552/566 of query aligns to 17:533/542 of O24146
- S189 (≠ T215) binding
- S190 (≠ G216) binding
- G191 (= G217) binding
- T192 (= T218) binding
- T193 (= T219) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K223) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H262) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y264) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ F268) binding ; binding ; binding
- K260 (≠ P286) binding
- A309 (≠ G335) binding ; binding ; binding
- Q331 (≠ E356) binding
- G332 (= G357) binding ; binding ; binding ; binding ; binding
- T336 (= T361) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V366) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D439) binding ; binding ; binding ; binding ; binding
- R435 (= R454) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K456) binding ; binding ; binding ; binding
- K441 (≠ L460) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S462) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G463) binding
- Q446 (≠ N465) binding
- K526 (= K545) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 94% coverage: 20:552/566 of query aligns to 10:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K545)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H262), Y232 (= Y264), S236 (≠ F268), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), G327 (= G359), M328 (= M360), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 94% coverage: 20:552/566 of query aligns to 10:526/529 of 5bsuA